Extreme heat- and pressure-resistant 7-kDa protein P2 from the archaeon Sulfolobus solfataricus is dramatically destabilized by a single-point amino acid substitution

Proteins: Structure, Function and Genetics

Volumn 29, Issue 3, 1997, Pages 381-390

  Fusi, Paola ^a   Goossens, Koen ^b   Consonni, Roberto ^c   Grisa, Margareth ^a   Puricelli, Paola ^a   Vecchio, Giuseppe ^c   Vanoni, Marco ^a   Zetta, Lucia ^c   Heremans, Karel ^b   Tortora, Paolo ^a,d  

^a UNIVERSITY OF MILAN   (Italy)

^b UNIVERSITY OF LEUVEN   (Belgium)

^c CNR   (Italy)

^d Dipto Fisiol e Biochim Generali   (Italy)

Author keywords

Circular dichroism; Fourier transform infrared spectroscopy; Hydrostatic pressure; Nuclear magnetic resonance; Piezostability; Site directed mutagenesis; Thermostability

Indexed keywords

BACTERIAL PROTEIN; PROTEIN P2; UNCLASSIFIED DRUG;

AMINO ACID SUBSTITUTION; ARTICLE; GENE CLUSTER; HEAT TOLERANCE; MOLECULAR CLONING; NONHUMAN; PRESSURE MEASUREMENT; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DENATURATION; PROTEIN ISOLATION; STRUCTURE ANALYSIS;

ALANINE; AMINO ACID SUBSTITUTION; ARCHAEAL PROTEINS; DNA-BINDING PROTEINS; HEAT; PHENYLALANINE; POINT MUTATION; PRESSURE; PROTEIN FOLDING; RECOMBINANT FUSION PROTEINS; RIBONUCLEASES; SULFOLOBUS;

EID: 0030781508     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0134(199711)29:3<381::AID-PROT11>3.0.CO;2-J     Document Type: Article

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